Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.

Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran. CRM1-mediated export is regulated by RanBP3, a Ran-interacting nuclear protein....

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Autores principales:	Karla Langer, Cyril Dian, Vladimir Rybin, Christoph W Müller, Carlo Petosa
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3d55aeaee9074e3dbf7009174baa43af
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spelling	oai:doaj.org-article:3d55aeaee9074e3dbf7009174baa43af2021-11-18T06:58:09ZInsights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.1932-620310.1371/journal.pone.0017011https://doaj.org/article/3d55aeaee9074e3dbf7009174baa43af2011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21364925/?tool=EBIhttps://doaj.org/toc/1932-6203Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran. CRM1-mediated export is regulated by RanBP3, a Ran-interacting nuclear protein. Unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, RanBP3 acts as a CRM1 cofactor, enhancing NES export by stabilizing the export complex in the nucleus. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. Here we report the crystal structure of the Ran-binding domain (RBD) from RanBP3 and compare it to RBD structures from RanBP1 and RanBP2 in complex with Ran and CRM1. Differences among these structures suggest why RanBP3 binds Ran with unusually low affinity, how RanBP3 modulates the cargo selectivity of CRM1, and why RanBP3 promotes assembly rather than disassembly of the export complex. The comparison of RBD structures thus provides an insight into the functional diversity of Ran-binding proteins.Karla LangerCyril DianVladimir RybinChristoph W MüllerCarlo PetosaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 2, p e17011 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Karla Langer Cyril Dian Vladimir Rybin Christoph W Müller Carlo Petosa Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
description	Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran. CRM1-mediated export is regulated by RanBP3, a Ran-interacting nuclear protein. Unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, RanBP3 acts as a CRM1 cofactor, enhancing NES export by stabilizing the export complex in the nucleus. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. Here we report the crystal structure of the Ran-binding domain (RBD) from RanBP3 and compare it to RBD structures from RanBP1 and RanBP2 in complex with Ran and CRM1. Differences among these structures suggest why RanBP3 binds Ran with unusually low affinity, how RanBP3 modulates the cargo selectivity of CRM1, and why RanBP3 promotes assembly rather than disassembly of the export complex. The comparison of RBD structures thus provides an insight into the functional diversity of Ran-binding proteins.
format	article
author	Karla Langer Cyril Dian Vladimir Rybin Christoph W Müller Carlo Petosa
author_facet	Karla Langer Cyril Dian Vladimir Rybin Christoph W Müller Carlo Petosa
author_sort	Karla Langer
title	Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
title_short	Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
title_full	Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
title_fullStr	Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
title_full_unstemmed	Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
title_sort	insights into the function of the crm1 cofactor ranbp3 from the structure of its ran-binding domain.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/3d55aeaee9074e3dbf7009174baa43af
work_keys_str_mv	AT karlalanger insightsintothefunctionofthecrm1cofactorranbp3fromthestructureofitsranbindingdomain AT cyrildian insightsintothefunctionofthecrm1cofactorranbp3fromthestructureofitsranbindingdomain AT vladimirrybin insightsintothefunctionofthecrm1cofactorranbp3fromthestructureofitsranbindingdomain AT christophwmuller insightsintothefunctionofthecrm1cofactorranbp3fromthestructureofitsranbindingdomain AT carlopetosa insightsintothefunctionofthecrm1cofactorranbp3fromthestructureofitsranbindingdomain
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Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.

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